The reaction of alternate oxidants with cytochrome P450BM3 and mutants generates spectrally detectable, high valent iron intermediates
- UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
- Jonathan Ira Thompson (Creator)
- Institution
- The University of North Carolina at Greensboro (UNCG )
- Web Site: http://library.uncg.edu/
- Advisor
- Gregory Raner
Abstract: "The Cytochrome P450 family serves as the forefront for xenobiotic metabolism in the human body. An understanding of the mechanism behind this enzyme family is a necessity for later research in the areas of pharmaceuticals and biochemistry. It has been observed by previous researchers that the transient species compound I, a highly reactive π-cation radical intermediate, is able to be viewed with P450cam and other heme containing proteins with subjection to various oxidant compounds such as m-CPBA or peracetic acid. In this study Cytochrome P450BM3 and its' heme domain, P450BMH, has been reacted with various oxidant compounds to show evidence of this compound I intermediate by diode array spectrophotometry and electron paramagnetic resonance spectroscopy."--Abstract from author supplied metadata.
The reaction of alternate oxidants with cytochrome P450BM3 and mutants generates spectrally detectable, high valent iron intermediates
PDF (Portable Document Format)
868 KB
Created on 12/1/2006
Views: 1585
Additional Information
- Publication
- Thesis
- Language: English
- Date: 2006
- Keywords
- Cytochrome P450, xenobiotic metabolism, pharmaceuticals, biochemistry
- Subjects
- Cytochrome P-450
- Spectrophotometry